ArticleProtein science : a publication of the Protein Society2023
Development of bright red-shifted miRFP704nano using structural analysis of miRFPnano proteins.
Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 7 citations in OpenAlex.
- An ultralow-background far-red light-responsive optogenetic tool based on an engineered biliverdin-binding domain.Nature methods · 2026Article
- Bright monomeric fluorescent protein elite-niRFP704 for two-channel near-infrared STED nanoscopy.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Red-to-Near-Infrared Fluorescence Resonance Energy Transfer Reporters for Dual Imaging Applications.Small methods · 2026Article
- Mechanisms of Red-Shifted Absorption in Biliverdin-Binding Proteins.Biochemistry · 2026Article
- Synthetic multicolor antigen-stabilizable nanobody platform for intersectional labeling and functional imaging.Nature methods · 2026Article
- Synthetic multicolor antigen-stabilizable nanobody platform for intersectional labelling and functional imaging.bioRxiv : the preprint server for biology · 2025Article
- Integrated Study of Fluorescence Enhancement in the Y176H Variant of Cyanobacterial Phytochrome Cph1.Biochemistry · 2025Article
- Cyanobacteriochromes: A Rainbow of Photoreceptors.Annual review of microbiology · 2024Review
- High Fluorescence of Phytochromes Does Not Require Chromophore Protonation.Molecules (Basel, Switzerland) · 2024Article
- Destabilized near-infrared fluorescent nanobodies enable background-free targeting of GFP-based biosensors for imaging and manipulation.Nature communications · 2024Article
- Development of bright red-shifted miRFP704nano using structural analysis of miRFPnano proteins.Protein science : a publication of the Protein Society · 2023Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
We recently converted the GAF domain of NpR3784 cyanobacteriochrome into near-infrared (NIR) fluorescent proteins (FPs). Unlike cyanobacterichrome, which incorporates phycocyanobilin tetrapyrrole, engineered NIR FPs bind biliverdin abundant in mammalian cells, thus being the smallest scaffold for it. Here, we determined the crystal structure of the brightest blue-shifted protein of the series, miRFP670nano3, at 1.8 Å resolution, characterized its chromophore environment and explained the molecular basis of its spectral properties. Using the determined structure, we have rationally designed a red-shifted NIR FP, termed miRFP704nano, with excitation at 680 nm and emission at 704 nm. miRFP704nano exhibits a small size of 17 kDa, enhanced molecular brightness, photostability and pH-stability. miRFP704nano performs well in various protein fusions in live mammalian cells and should become a versatile genetically-encoded NIR probe for multiplexed imaging across spatial scales in different modalities.
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Registered trials
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